4v81

The crystal structure of yeast CCT reveals intrinsic asymmetry of eukaryotic cytosolic chaperoninsThe crystal structure of yeast CCT reveals intrinsic asymmetry of eukaryotic cytosolic chaperonins

Structural highlights 4v81 is a 32 chain structure with sequence from Saccharomyces cerevisiae. This structure supersedes the now removed PDB entries 3p9d and 3p9e. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.8Å Ligands: , , Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function TCPA_YEAST Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. In yeast may play a role in mitotic spindle formation. Publication Abstract from PubMed The cytosolic chaperonin CCT is a 1-MDa protein-folding machine essential for eukaryotic life. The CCT interactome shows involvement in folding and assembly of a small range of proteins linked to essential cellular processes such as cytoskeleton assembly and cell-cycle regulation. CCT has a classic chaperonin architecture, with two heterogeneous 8-membered rings stacked back-to-back, enclosing a folding cavity. However, the mechanism by which CCT assists folding is distinct from other chaperonins, with no hydrophobic wall lining a potential Anfinsen cage, and a sequential rather than concerted ATP hydrolysis mechanism. We have solved the crystal structure of yeast CCT in complex with actin at 3.8 A resolution, revealing the subunit organisation and the location of discrete patches of co-evolving 'signature residues' that mediate specific interactions between CCT and its substrates. The intrinsic asymmetry is revealed by the structural individuality of the CCT subunits, which display unique configurations, substrate binding properties, ATP-binding heterogeneity and subunit-subunit interactions. The location of the evolutionarily conserved N-terminus of Cct5 on the outside of the barrel, confirmed by mutational studies, is unique to eukaryotic cytosolic chaperonins. The crystal structure of yeast CCT reveals intrinsic asymmetry of eukaryotic cytosolic chaperonins.,Dekker C, Roe SM, McCormack EA, Beuron F, Pearl LH, Willison KR EMBO J. 2011 Jun 24. doi: 10.1038/emboj.2011.208. PMID:21701561 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Chaperonin 3D structures

spinqualitylabelsall models 4v81, resolution 3.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image